ID A0A1T5FLE0_9MICC Unreviewed; 417 AA.
AC A0A1T5FLE0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:SKB96989.1};
GN ORFNames=SAMN05660473_03364 {ECO:0000313|EMBL:SKB96989.1};
OS Arthrobacter sp. 49Tsu3.1M3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1279029 {ECO:0000313|EMBL:SKB96989.1, ECO:0000313|Proteomes:UP000189904};
RN [1] {ECO:0000313|EMBL:SKB96989.1, ECO:0000313|Proteomes:UP000189904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49Tsu3.1M3 {ECO:0000313|EMBL:SKB96989.1,
RC ECO:0000313|Proteomes:UP000189904};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUZD01000018; SKB96989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5FLE0; -.
DR Proteomes; UP000189904; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:SKB96989.1}.
FT DOMAIN 83..351
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 44629 MW; 0E979BDA668B3D6D CRC64;
MTISADHAAQ PAAQQAAQQD PAGDAVSKFG ITVEDYMLPA RHQIQMVGPD GTLNPHTEQG
TQPGHEYSLP SEAELMAAYE QLVIGRRVND QNSALVRQGR MAVYPSSHGQ EACQVAAALC
LAEGDWLFPT YRDSVAVMAR GVDPVQTMTL FRGDWHGGYD PAKNKVGIQC TPLTTQLLHG
VGVAHAAKLR GEDTVVLAMC GDGATSEGDF HEALNFAAVF HLPVVFFVQN NQYAISVPLA
HQSVAPSLAH KAVGYGMAGE RVDGNDIVAL LAVLGRAVKL AREGSGPLLV EAHTYRMQAH
TNADDATRYR QDSEVAEWVA KDPLSRMQTY LTDRGLLDDD RAAAIAEKAE AVATQLREGL
SEEVPVEPQD LFKYVFSTPT PQLKEQSAML ADELARDAAS TATASAAATS ISREAGI
//